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The enzyme Pimelyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85, BioH; systematic name pimelyl-[acyl-carrier protein] methyl ester hydrolase ...
The enzyme protein-glutamate methylesterase (EC 3.1.1.61) catalyzes the reaction . protein L-glutamate O 5-methyl ester + H 2 O protein L-glutamate + methanol. This enzyme is a demethylase, and more specifically it belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds.
The enzyme protein phosphatase methylesterase-1 (EC 3.1.1.89, PME-1, PPME1; systematic name (phosphatase 2A protein)-leucine ester acylhydrolase [1] [2] catalyses the reaction [phosphatase 2A protein]-leucine methyl ester + H 2 O ⇌ {\displaystyle \rightleftharpoons } [phosphatase 2A protein]-leucine + methanol
Transesterification is the process of exchanging the organic functional group R″ of an ester with the organic group R' of an alcohol. These reactions are often catalyzed by the addition of an acid or base catalyst. [1] Strong acids catalyze the reaction by donating a proton to the carbonyl group, thus making it a more potent electrophile.
An ester of carboxylic acid. R stands for any group (organic or inorganic) and R′ stands for organyl group. In chemistry, an ester is a compound derived from an acid (organic or inorganic) in which the hydrogen atom (H) of at least one acidic hydroxyl group (−OH) of that acid is replaced by an organyl group (−R).
Methylation is catalysed by CheR, an S-adenosylmethionine-dependent methyltransferase, [1] which reversibly methylates specific glutamate residues within a coiled coil region, to form gamma-glutamyl methyl ester residues. [1] [2] The structure of the Salmonella typhimurium chemotaxis receptor methyltransferase CheR, bound to S ...
One pathway utilizes a Δ 9-desaturase (DesA) that catalyzes a double bond formation in membrane lipids. Another pathway uses two proteins, DesC and DesB, together to act as a Δ 9-desaturase, which inserts a double bond into a saturated fatty acid-CoA molecule. This second pathway is regulated by repressor protein DesT.
The molecule folds into 2 domains, an N-terminal catalytic domain, which contains the catalytic and cofactor binding sites, and comprises a central 9-stranded beta-sheet, surrounded by 5 helices; and a C-terminal DNA recognition domain, which is formed by 4 small beta-sheets and 8 alpha-helices.